Ontology highlight
ABSTRACT:
SUBMITTER: Saksouk N
PROVIDER: S-EPMC2677731 | biostudies-literature | 2009 Jan
REPOSITORIES: biostudies-literature
Saksouk Nehmé N Avvakumov Nikita N Champagne Karen S KS Hung Tiffany T Doyon Yannick Y Cayrou Christelle C Paquet Eric E Ullah Mukta M Landry Anne-Julie AJ Côté Valérie V Yang Xiang-Jiao XJ Gozani Or O Kutateladze Tatiana G TG Côté Jacques J
Molecular cell 20090101 2
The HBO1 HAT protein is the major source of histone H4 acetylation in vivo and has been shown to play critical roles in gene regulation and DNA replication. A distinctive characteristic of HBO1 HAT complexes is the presence of three PHD finger domains in two different subunits: tumor suppressor proteins ING4/5 and JADE1/2/3. Biochemical and functional analyses indicate that these domains interact with histone H3 N-terminal tail region, but with a different specificity toward its methylation stat ...[more]